4hil

1.25A Resolution Structure of Rat Type B Cytochrome b5

Method: X-RAY DIFFRACTION Dmax: 54.8 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Cytochrome b5 type B

Rattus norvegicus

UniProt P04166

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 17–102 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;293 K;30% (w/v) PEG 8000, 100 sodium cacodylate, 200 mM sodium acetate, pH 6.5, vapor diffusion, temperature 293K Resolution 1.25 Å R-free 0.152
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 17–102 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;293 K;30% (w/v) PEG 8000, 100 sodium cacodylate, 200 mM sodium acetate, pH 6.5, vapor diffusion, temperature 293K Resolution 1.25 Å R-free 0.152

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYB5B_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–86; UniProt 17–102 Author chain B; PDBConstruct 1–86; UniProt 17–102

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 4hil

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4hil
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4hil
Deposition date deposition_date2012-10-11
Structure title title1.25A Resolution Structure of Rat Type B Cytochrome b5
Keywords keywordsCYTOCHROME B5, HEME, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.41
Radius of gyration Rg (electron density) rg_electron16.42
Forward intensity I(0) i07641330.00
Molecular weight molecular_weight20045.0 kDa
Excluded volume excluded_volume24886 ų
Envelope volume envelope_volume28232 ų
Hydration-shell volume shell_volume14832 ų
Envelope diameter envelope_diameter55.4
Shell Rg shell_rg21.86
Envelope Rg envelope_rg16.50
Shape Rg shape_rg16.41
Total Rg total_rg17.40
Total atoms total_atoms1415
Residues n_residues166
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax54.8
Rg (real space) rg_real17.34
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real7.6410e+06
I(0) uncertainty (real space) i0_real_error8.0340e+04
Rg (reciprocal space) rg_reciprocal17.35
I(0) (reciprocal space) i0_reciprocal7641000.0000
Solution quality estimate total_estimate0.8185
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.2
Skewness Skewness skewness0.232
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2011000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4hila_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.120 — Cytochrome b5-like heme/steroid binding domain
Superfamily Superfamily superfamilyd.120.1 — Cytochrome b5-like heme/steroid binding domain
Family Family familyd.120.1.1 — Cytochrome b5
Domain ID domain_idd4hilb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.120 — Cytochrome b5-like heme/steroid binding domain
Superfamily Superfamily superfamilyd.120.1 — Cytochrome b5-like heme/steroid binding domain
Family Family familyd.120.1.1 — Cytochrome b5

CATH v4.4 (2 domains)

Domain ID domain_id4hilA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology120 — Flavocytochrome B2; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Cytochrome b5-like heme/steroid binding domain
Domain ID domain_id4hilB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology120 — Flavocytochrome B2; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Cytochrome b5-like heme/steroid binding domain

8. Citations (1)

9. Files and Curves (10)